Enzyme kinetics models how free enzyme, substrate, enzyme-substrate complexes, and product concentrations evolve through a reaction mechanism.
The Michaelis-Menten rate law is
It is linear at low substrate concentration and saturates at at high concentration.
When enzyme complexes relax much faster than substrate concentrations, the quasi-steady-state approximation sets the time derivatives of the fast complexes to zero and solves their algebraic balance equations.
For sequential binding with dimensionless parameters , the reduced product rate has the form
It is quadratic at low substrate concentration and saturates at high concentration.

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Enzyme kinetics is the study of the rates of enzyme-catalyzed reactions and how various factors influence those rates. It provides insights into the biochemical processes involved in cellular metabolism and other biological functions where enzymes play critical roles. Key concepts in enzyme kinetics include: 1. **Reaction Rate**: The speed at which a substrate is converted to product by an enzyme.